Production, purification, crystallization and preliminary X-ray analysis of adeno-associated virus serotype 8

Michael Douglas Lane, Hyun Joo Nam, Eric Padron, Brittney Gurda-Whitaker, Eric Kohlbrenner, George Aslanidi, Barry Byrne, Robert McKenna, Nicholas Muzyczka, Sergei Zolotukhin, Mavis Agbandje-McKenna

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Abstract

Adeno-associated viruses (AAVs) are actively being developed for clinical gene-therapy applications and the efficiencies of the vectors could be significantly improved by a detailed understanding of their viral capsid structures and the structural determinants of their tissue-transduction interactions. AAV8 is ∼80% identical to the more widely studied AAV2, but its liver-transduction efficiency is significantly greater than that of AAV2 and other serotypes. The production, purification, crystallization and preliminary X-ray crystallographic analysis of AAV8 viral capsids are reported. The crystals diffract X-rays to 3.0 Å resolution using synchrotron radiation and belong to the hexagonal space group P6322, with unit-cell parameters a = 257.5, c = 443.5 Å. The unit cell contains two viral particles, with ten capsid viral protein monomers per crystallographic asymmetric unit.

Original languageEnglish (US)
Pages (from-to)558-561
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number6
DOIs
StatePublished - 2005

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    Lane, M. D., Nam, H. J., Padron, E., Gurda-Whitaker, B., Kohlbrenner, E., Aslanidi, G., Byrne, B., McKenna, R., Muzyczka, N., Zolotukhin, S., & Agbandje-McKenna, M. (2005). Production, purification, crystallization and preliminary X-ray analysis of adeno-associated virus serotype 8. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61(6), 558-561. https://doi.org/10.1107/S1744309105014132